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High avidity scFv multimers; diabodies and triabodies.
1CSIRO Molecular Science and CRC for Diagnostic Technologies, 343 Royal Parade, Parkville, Victoria, 3052, Australia. peter.hudson@molsci.csiro.au
Journal of Immunological Methods
|January 29, 2000
Summary
Engineered antibody fragments, called single chain Fv multimers, offer enhanced tumor targeting and clearance. Varying linker lengths control multimer size, improving in vivo imaging and therapy applications.
Area of Science:
- Biotechnology
- Immunology
- Molecular Biology
Background:
- Multivalent recombinant antibody fragments offer high binding avidity and specificity.
- Single chain Fv (scFv) fragments can be engineered into multimers with tailored properties.
Purpose of the Study:
- To review the design of multivalent and multispecific Fv modules.
- To explore their applications in vivo imaging, therapy, and diagnostics.
Main Methods:
- Engineering scFv fragments with varying linker lengths to form dimers, trimers, and tetramers.
- Assessing the impact of linker length on Fv module size, flexibility, and valency.
- Designing multispecific Fv modules for specific applications like T-cell recruitment.
Main Results:
- Linker length dictates scFv multimerization (diabodies, triabodies, tetramers).
- scFv multimers exhibit high avidity due to increased binding valency.
- Molecules of 60-100 kDa show improved tumor penetration and clearance rates.
Conclusions:
- Engineered scFv multimers provide tunable size, flexibility, and valency for diverse applications.
- These constructs are promising for in vivo imaging, cancer therapy, and immunodiagnostics.
- Multispecific multimers enable targeted cell recruitment and agglutination.